7T7J

Crystal Structure of Phosphoserine aminotransferase from Klebsiella pneumoniae subsp. pneumoniae in complex with Pyridoxal phosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
A	0005737	cellular_component	cytoplasm
A	0006563	biological_process	L-serine metabolic process
A	0006564	biological_process	L-serine biosynthetic process
A	0008483	molecular_function	transaminase activity
A	0008615	biological_process	pyridoxine biosynthetic process
A	0008652	biological_process	amino acid biosynthetic process
A	0016740	molecular_function	transferase activity
A	0030170	molecular_function	pyridoxal phosphate binding
B	0004648	molecular_function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity
B	0005737	cellular_component	cytoplasm
B	0006563	biological_process	L-serine metabolic process
B	0006564	biological_process	L-serine biosynthetic process
B	0008483	molecular_function	transaminase activity
B	0008615	biological_process	pyridoxine biosynthetic process
B	0008652	biological_process	amino acid biosynthetic process
B	0016740	molecular_function	transferase activity
B	0030170	molecular_function	pyridoxal phosphate binding

Functional Information from PROSITE/UniProt

site_id	PS00595
Number of Residues	20
Details	AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. FGVIyaGAQKnigpa.GlTlV

Chain	Residue	Details
A	PHE189-VAL208

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00160","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00160","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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